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Article

Methionine Adenosyltransferase Engineering to Enable Bioorthogonal Platforms for AdoMet-Utilizing Enzymes.

ACS chemical biology - 20 Mar 2020

Huber Tyler D, Clinger Jonathan A, Liu Yang, Xu Weijun, Miller Mitchell D, Phillips George N, Thorson Jon S

Abstract excerpt

The structural conservation among methyltransferases (MTs) and MT functional redundancy is a major challenge to the cellular study of individual MTs. As a first step toward the development of an alternative biorthogonal platform for MTs and other AdoMet-utilizing enzymes, we describe the evaluation of 38 human methionine adenosyltransferase II-α (hMAT2A) mutants in combination with 14 non-native methionine...

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Identifiers

PMID: 32091873
DOI: 10.1021/acschembio.9b00943
PMCID: PMC7516136

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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